Enzymes active in the areas undergoing cartilage resorption during the development of the secondary ossification center in the tibiae of rats aged 0–21 days. II. Two proteinases, gelatinase B and collagenase‐3, are implicated in the lysis of collagen fibrils

In the transformation of the cartilaginous epiphysis into bone, the first indication of change in the surfaces destined for resorption is the cleavage of aggrecan core protein by unidentified matrix metalloproteinases (MMPs) (Lee et al., this issue). In cartilage areas undergoing resorption, the cle...

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Veröffentlicht in:	Developmental dynamics 2001-09, Vol.222 (1), p.71-88
Hauptverfasser:	Davoli, Maria Antonietta, Lamplugh, Lisa, Beauchemin, Annie, Chan, Kevin, Mordier, Sylvie, Mort, John S., Murphy, Gillian, Docherty, Andrew J.P., Leblond, Charles Philippe, Lee, Eunice R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Biotinylation Bone and Bones - embryology Bone and Bones - ultrastructure Bone Resorption Cartilage - enzymology Cartilage - physiology cartilage lysis Collagen - metabolism Collagenases - metabolism collagenase‐3 Electrophoresis, Polyacrylamide Gel Enzyme Inhibitors - pharmacology Epiphyses - metabolism Gelatin - metabolism gelatinase B Immunoglobulin G - metabolism Immunohistochemistry Male Matrix Metalloproteinase 13 Matrix Metalloproteinase 9 - metabolism Matrix Metalloproteinase Inhibitors matrix metalloproteinases Matrix Metalloproteinases - metabolism Microscopy, Electron Microscopy, Immunoelectron Rats Rats, Sprague-Dawley skeletal development Time Factors Tissue Inhibitor of Metalloproteinase-1 - pharmacology Tissue Inhibitor of Metalloproteinase-2 - metabolism Tissue Inhibitor of Metalloproteinase-2 - pharmacology vascular invasion zymography
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